Research workbench
Crystal structure of the C-terminal half of the vibrio cholerae minor pilin tcpb
Analyse Crystal structure of the C-terminal half of the vibrio cholerae minor pilin tcpb in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MIC
- Type
- protein
- Length
- 164 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Toxin co-regulated pilus biosynthesis protein B
- UniProt
- A0A0H3AKH0
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Toxin co-regulated pilus biosynthesis protein B | protein | 164 | 0% helix, 48% strand | A0A0H3AKH0 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 6MIC · Crystal Structure of the C-terminal half of the Vibrio cholerae minor pilin TcpB · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A0A0H3AKH0
- Elsewhere: RCSB PDB 6MIC · PDBe 6MIC · UniProt A0A0H3AKH0
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